HEADER NUCLEAR PROTEIN 23-SEP-23 8UBI TITLE CRYO-EM STRUCTURE OF NRCAM NUCLEOSOME AIDED BY SCFV (CLASS_A) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HISTONE H3; COMPND 3 CHAIN: A, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HISTONE H4; COMPND 7 CHAIN: B, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HISTONE H2A; COMPND 11 CHAIN: C, G; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HISTONE H2B TYPE 1-J; COMPND 15 CHAIN: D, H; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: NRCAM DNA (162-MER); COMPND 19 CHAIN: I; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: NRCAM DNA (162-MER); COMPND 23 CHAIN: J; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 7; COMPND 26 MOLECULE: SCFV; COMPND 27 CHAIN: M, N; COMPND 28 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CR201_G0042554; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 GENE: E5288_WYG010732; SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 GENE: H2BC11; SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 28 MOL_ID: 5; SOURCE 29 SYNTHETIC: YES; SOURCE 30 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 31 ORGANISM_TAXID: 10090; SOURCE 32 MOL_ID: 6; SOURCE 33 SYNTHETIC: YES; SOURCE 34 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 35 ORGANISM_TAXID: 10090; SOURCE 36 MOL_ID: 7; SOURCE 37 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 38 ORGANISM_TAXID: 10090; SOURCE 39 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NUCLEOSOME, PIONEER TRANSCRIPTION FACTORS, DNA BINDING PROTEINS, KEYWDS 2 TRANSCRIPTION, NUCLEAR PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR B.R.ZHOU,Y.BAI REVDAT 1 21-JAN-26 8UBI 0 JRNL AUTH B.R.ZHOU,Y.BAI JRNL TITL CRYO-EM STRUCTURE OF NRCAM NUCLEOSOME AIDED BY SCFV JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.800 REMARK 3 NUMBER OF PARTICLES : 63842 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8UBI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-23. REMARK 100 THE DEPOSITION ID IS D_1000277730. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : 162BP NRCAM NUCLEOSOME IN REMARK 245 COMPLEX WITH SCFV REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 100.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: M, N REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET M 0 REMARK 465 LYS M 1 REMARK 465 SER M 2 REMARK 465 SER M 3 REMARK 465 HIS M 4 REMARK 465 HIS M 5 REMARK 465 HIS M 6 REMARK 465 HIS M 7 REMARK 465 HIS M 8 REMARK 465 HIS M 9 REMARK 465 GLU M 10 REMARK 465 ASN M 11 REMARK 465 LEU M 12 REMARK 465 TYR M 13 REMARK 465 PHE M 14 REMARK 465 GLN M 15 REMARK 465 SER M 16 REMARK 465 ASN M 17 REMARK 465 ALA M 18 REMARK 465 ARG M 127 REMARK 465 ALA M 128 REMARK 465 GLY M 129 REMARK 465 GLY M 130 REMARK 465 GLY M 131 REMARK 465 GLY M 132 REMARK 465 SER M 133 REMARK 465 GLY M 134 REMARK 465 GLY M 135 REMARK 465 GLY M 136 REMARK 465 GLY M 137 REMARK 465 SER M 138 REMARK 465 GLY M 139 REMARK 465 GLY M 140 REMARK 465 GLY M 141 REMARK 465 GLY M 142 REMARK 465 SER M 143 REMARK 465 GLY M 144 REMARK 465 GLY M 145 REMARK 465 GLY M 146 REMARK 465 GLY M 147 REMARK 465 SER M 148 REMARK 465 MET M 149 REMARK 465 SER M 269 REMARK 465 MET N 0 REMARK 465 LYS N 1 REMARK 465 SER N 2 REMARK 465 SER N 3 REMARK 465 HIS N 4 REMARK 465 HIS N 5 REMARK 465 HIS N 6 REMARK 465 HIS N 7 REMARK 465 HIS N 8 REMARK 465 HIS N 9 REMARK 465 GLU N 10 REMARK 465 ASN N 11 REMARK 465 LEU N 12 REMARK 465 TYR N 13 REMARK 465 PHE N 14 REMARK 465 GLN N 15 REMARK 465 SER N 16 REMARK 465 ASN N 17 REMARK 465 ALA N 18 REMARK 465 ARG N 127 REMARK 465 ALA N 128 REMARK 465 GLY N 129 REMARK 465 GLY N 130 REMARK 465 GLY N 131 REMARK 465 GLY N 132 REMARK 465 SER N 133 REMARK 465 GLY N 134 REMARK 465 GLY N 135 REMARK 465 GLY N 136 REMARK 465 GLY N 137 REMARK 465 SER N 138 REMARK 465 GLY N 139 REMARK 465 GLY N 140 REMARK 465 GLY N 141 REMARK 465 GLY N 142 REMARK 465 SER N 143 REMARK 465 GLY N 144 REMARK 465 GLY N 145 REMARK 465 GLY N 146 REMARK 465 GLY N 147 REMARK 465 SER N 148 REMARK 465 MET N 149 REMARK 465 SER N 269 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 DC I 58 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES REMARK 500 DC I 99 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES REMARK 500 DC J 5 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES REMARK 500 DT J 33 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES REMARK 500 DG J 42 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES REMARK 500 DT J 53 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES REMARK 500 DT J 63 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES REMARK 500 DG J 114 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES REMARK 500 DG J 144 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA M 70 -8.58 73.47 REMARK 500 ALA M 103 -177.96 -170.10 REMARK 500 ILE M 197 -62.00 -92.35 REMARK 500 ALA N 70 -10.38 73.30 REMARK 500 ASN N 95 -60.65 -92.31 REMARK 500 THR N 165 -169.03 -79.64 REMARK 500 ILE N 197 -61.56 -93.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-42089 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF NRCAM NUCLEOSOME AIDED BY SCFV (CLASS_A) DBREF 8UBI A 37 133 UNP H2PI50 H2PI50_PONAB 38 134 DBREF1 8UBI B 20 102 UNP A0A9J8D176_CYPCA DBREF2 8UBI B A0A9J8D176 10 92 DBREF 8UBI C 10 118 UNP L8IQP7 L8IQP7_9CETA 11 119 DBREF 8UBI D 30 124 UNP P06899 H2B1J_HUMAN 31 125 DBREF 8UBI E 37 133 UNP H2PI50 H2PI50_PONAB 38 134 DBREF1 8UBI F 20 102 UNP A0A9J8D176_CYPCA DBREF2 8UBI F A0A9J8D176 10 92 DBREF 8UBI G 10 118 UNP L8IQP7 L8IQP7_9CETA 11 119 DBREF 8UBI H 30 124 UNP P06899 H2B1J_HUMAN 31 125 DBREF 8UBI I 1 162 PDB 8UBI 8UBI 1 162 DBREF 8UBI J 1 162 PDB 8UBI 8UBI 1 162 DBREF 8UBI M 0 269 PDB 8UBI 8UBI 0 269 DBREF 8UBI N 0 269 PDB 8UBI 8UBI 0 269 SEQRES 1 A 97 LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG SEQRES 2 A 97 GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE SEQRES 3 A 97 ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA SEQRES 4 A 97 GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA SEQRES 5 A 97 VAL MET ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL SEQRES 6 A 97 GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA SEQRES 7 A 97 LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA SEQRES 8 A 97 ARG ARG ILE ARG GLY GLU SEQRES 1 B 83 LYS VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO SEQRES 2 B 83 ALA ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG SEQRES 3 B 83 ILE SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU SEQRES 4 B 83 LYS VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR SEQRES 5 B 83 TYR THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET SEQRES 6 B 83 ASP VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU SEQRES 7 B 83 TYR GLY PHE GLY GLY SEQRES 1 C 109 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY SEQRES 2 C 109 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG SEQRES 3 C 109 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO SEQRES 4 C 109 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU SEQRES 5 C 109 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS SEQRES 6 C 109 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE SEQRES 7 C 109 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL SEQRES 8 C 109 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA SEQRES 9 C 109 VAL LEU LEU PRO LYS SEQRES 1 D 95 LYS ARG SER ARG LYS GLU SER TYR SER ILE TYR VAL TYR SEQRES 2 D 95 LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SEQRES 3 D 95 SER LYS ALA MET GLY ILE MET ASN SER PHE VAL ASN ASP SEQRES 4 D 95 ILE PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU ALA SEQRES 5 D 95 HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE SEQRES 6 D 95 GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA SEQRES 7 D 95 LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS SEQRES 8 D 95 TYR THR SER ALA SEQRES 1 E 97 LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG SEQRES 2 E 97 GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE SEQRES 3 E 97 ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA SEQRES 4 E 97 GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA SEQRES 5 E 97 VAL MET ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL SEQRES 6 E 97 GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA SEQRES 7 E 97 LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA SEQRES 8 E 97 ARG ARG ILE ARG GLY GLU SEQRES 1 F 83 LYS VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO SEQRES 2 F 83 ALA ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG SEQRES 3 F 83 ILE SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU SEQRES 4 F 83 LYS VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR SEQRES 5 F 83 TYR THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET SEQRES 6 F 83 ASP VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU SEQRES 7 F 83 TYR GLY PHE GLY GLY SEQRES 1 G 109 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY SEQRES 2 G 109 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG SEQRES 3 G 109 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO SEQRES 4 G 109 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU SEQRES 5 G 109 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS SEQRES 6 G 109 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE SEQRES 7 G 109 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL SEQRES 8 G 109 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA SEQRES 9 G 109 VAL LEU LEU PRO LYS SEQRES 1 H 95 LYS ARG SER ARG LYS GLU SER TYR SER ILE TYR VAL TYR SEQRES 2 H 95 LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SEQRES 3 H 95 SER LYS ALA MET GLY ILE MET ASN SER PHE VAL ASN ASP SEQRES 4 H 95 ILE PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU ALA SEQRES 5 H 95 HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE SEQRES 6 H 95 GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA SEQRES 7 H 95 LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS SEQRES 8 H 95 TYR THR SER ALA SEQRES 1 I 162 DG DA DT DC DC DA DT DT DA DC DT DT DC SEQRES 2 I 162 DT DG DA DA DA DC DA DG DA DT DG DA DC SEQRES 3 I 162 DT DC DC DC DA DG DC DA DG DC DT DG DC SEQRES 4 I 162 DT DG DC DC DT DG DT DG DG DC DC DC DA SEQRES 5 I 162 DC DA DG DG DG DC DT DT DC DC DT DG DC SEQRES 6 I 162 DC DC DT DG DC DA DT DG DA DC DA DG DC SEQRES 7 I 162 DT DG DC DA DC DA DT DC DA DC DA DT DC SEQRES 8 I 162 DC DT DG DT DG DG DT DC DA DT DA DC DT SEQRES 9 I 162 DA DC DT DT DC DA DG DC DC DG DC DT DT SEQRES 10 I 162 DC DT DA DC DG DG DC DC DA DG DA DT DA SEQRES 11 I 162 DC DA DA DA DA DG DT DG DG DG DT DG DG SEQRES 12 I 162 DG DG DA DA DC DA DT DA DG DG DC DA DA SEQRES 13 I 162 DG DG DG DA DT DC SEQRES 1 J 162 DG DA DT DC DC DC DT DT DG DC DC DT DA SEQRES 2 J 162 DT DG DT DT DC DC DC DC DA DC DC DC DA SEQRES 3 J 162 DC DT DT DT DT DG DT DA DT DC DT DG DG SEQRES 4 J 162 DC DC DG DT DA DG DA DA DG DC DG DG DC SEQRES 5 J 162 DT DG DA DA DG DT DA DG DT DA DT DG DA SEQRES 6 J 162 DC DC DA DC DA DG DG DA DT DG DT DG DA SEQRES 7 J 162 DT DG DT DG DC DA DG DC DT DG DT DC DA SEQRES 8 J 162 DT DG DC DA DG DG DG DC DA DG DG DA DA SEQRES 9 J 162 DG DC DC DC DT DG DT DG DG DG DC DC DA SEQRES 10 J 162 DC DA DG DG DC DA DG DC DA DG DC DT DG SEQRES 11 J 162 DC DT DG DG DG DA DG DT DC DA DT DC DT SEQRES 12 J 162 DG DT DT DT DC DA DG DA DA DG DT DA DA SEQRES 13 J 162 DT DG DG DA DT DC SEQRES 1 M 270 MET LYS SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU SEQRES 2 M 270 TYR PHE GLN SER ASN ALA MET ASP ILE LYS MET THR GLN SEQRES 3 M 270 SER PRO SER SER MET HIS ALA SER LEU GLY GLU ARG VAL SEQRES 4 M 270 THR ILE THR CYS LYS ALA SER GLN ASP ILE ARG SER TYR SEQRES 5 M 270 LEU SER TRP TYR GLN GLN LYS PRO TRP LYS SER PRO LYS SEQRES 6 M 270 THR LEU ILE TYR TYR ALA THR SER LEU ALA ASP GLY VAL SEQRES 7 M 270 PRO SER ARG PHE SER GLY SER GLY SER GLY GLN ASP PHE SEQRES 8 M 270 SER LEU THR ILE ASN ASN LEU GLU SER ASP ASP THR ALA SEQRES 9 M 270 THR TYR TYR CYS LEU GLN HIS GLY GLU SER PRO TYR THR SEQRES 10 M 270 PHE GLY SER GLY THR LYS LEU GLU ILE LYS ARG ALA GLY SEQRES 11 M 270 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 12 M 270 SER GLY GLY GLY GLY SER MET GLU VAL GLN LEU GLN GLN SEQRES 13 M 270 SER GLY PRO GLU LEU VAL GLU PRO GLY THR SER VAL LYS SEQRES 14 M 270 MET PRO CYS LYS ALA SER GLY TYR THR PHE THR SER TYR SEQRES 15 M 270 THR ILE GLN TRP VAL LYS GLN THR PRO ARG GLN GLY LEU SEQRES 16 M 270 GLU TRP ILE GLY TYR ILE TYR PRO TYR ASN ALA GLY THR SEQRES 17 M 270 LYS TYR ASN GLU LYS PHE LYS GLY LYS ALA THR LEU THR SEQRES 18 M 270 SER ASP LYS SER SER SER THR VAL TYR MET GLU LEU SER SEQRES 19 M 270 SER LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS ALA SEQRES 20 M 270 ARG LYS SER SER ARG LEU ARG SER THR LEU ASP TYR TRP SEQRES 21 M 270 GLY GLN GLY THR SER VAL THR VAL SER SER SEQRES 1 N 270 MET LYS SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU SEQRES 2 N 270 TYR PHE GLN SER ASN ALA MET ASP ILE LYS MET THR GLN SEQRES 3 N 270 SER PRO SER SER MET HIS ALA SER LEU GLY GLU ARG VAL SEQRES 4 N 270 THR ILE THR CYS LYS ALA SER GLN ASP ILE ARG SER TYR SEQRES 5 N 270 LEU SER TRP TYR GLN GLN LYS PRO TRP LYS SER PRO LYS SEQRES 6 N 270 THR LEU ILE TYR TYR ALA THR SER LEU ALA ASP GLY VAL SEQRES 7 N 270 PRO SER ARG PHE SER GLY SER GLY SER GLY GLN ASP PHE SEQRES 8 N 270 SER LEU THR ILE ASN ASN LEU GLU SER ASP ASP THR ALA SEQRES 9 N 270 THR TYR TYR CYS LEU GLN HIS GLY GLU SER PRO TYR THR SEQRES 10 N 270 PHE GLY SER GLY THR LYS LEU GLU ILE LYS ARG ALA GLY SEQRES 11 N 270 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 12 N 270 SER GLY GLY GLY GLY SER MET GLU VAL GLN LEU GLN GLN SEQRES 13 N 270 SER GLY PRO GLU LEU VAL GLU PRO GLY THR SER VAL LYS SEQRES 14 N 270 MET PRO CYS LYS ALA SER GLY TYR THR PHE THR SER TYR SEQRES 15 N 270 THR ILE GLN TRP VAL LYS GLN THR PRO ARG GLN GLY LEU SEQRES 16 N 270 GLU TRP ILE GLY TYR ILE TYR PRO TYR ASN ALA GLY THR SEQRES 17 N 270 LYS TYR ASN GLU LYS PHE LYS GLY LYS ALA THR LEU THR SEQRES 18 N 270 SER ASP LYS SER SER SER THR VAL TYR MET GLU LEU SER SEQRES 19 N 270 SER LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS ALA SEQRES 20 N 270 ARG LYS SER SER ARG LEU ARG SER THR LEU ASP TYR TRP SEQRES 21 N 270 GLY GLN GLY THR SER VAL THR VAL SER SER HELIX 1 AA1 GLY A 44 SER A 57 1 14 HELIX 2 AA2 ARG A 63 ASP A 77 1 15 HELIX 3 AA3 GLN A 85 ALA A 114 1 30 HELIX 4 AA4 MET A 120 GLY A 132 1 13 HELIX 5 AA5 ASN B 25 ILE B 29 5 5 HELIX 6 AA6 THR B 30 GLY B 41 1 12 HELIX 7 AA7 LEU B 49 ALA B 76 1 28 HELIX 8 AA8 THR B 82 GLN B 93 1 12 HELIX 9 AA9 THR C 16 GLY C 22 1 7 HELIX 10 AB1 PRO C 26 GLY C 37 1 12 HELIX 11 AB2 ALA C 45 ASN C 73 1 29 HELIX 12 AB3 ILE C 79 ASN C 89 1 11 HELIX 13 AB4 ASP C 90 LEU C 97 1 8 HELIX 14 AB5 GLN C 112 LEU C 116 5 5 HELIX 15 AB6 TYR D 37 HIS D 49 1 13 HELIX 16 AB7 SER D 55 ASN D 84 1 30 HELIX 17 AB8 THR D 90 LEU D 102 1 13 HELIX 18 AB9 PRO D 103 ALA D 124 1 22 HELIX 19 AC1 GLY E 44 SER E 57 1 14 HELIX 20 AC2 ARG E 63 GLN E 76 1 14 HELIX 21 AC3 GLN E 85 ALA E 114 1 30 HELIX 22 AC4 MET E 120 GLY E 132 1 13 HELIX 23 AC5 ASN F 25 ILE F 29 5 5 HELIX 24 AC6 THR F 30 GLY F 41 1 12 HELIX 25 AC7 LEU F 49 ALA F 76 1 28 HELIX 26 AC8 THR F 82 GLN F 93 1 12 HELIX 27 AC9 THR G 16 GLY G 22 1 7 HELIX 28 AD1 PRO G 26 GLY G 37 1 12 HELIX 29 AD2 ALA G 45 ASN G 73 1 29 HELIX 30 AD3 ILE G 79 ASN G 89 1 11 HELIX 31 AD4 ASP G 90 LEU G 97 1 8 HELIX 32 AD5 GLN G 112 LEU G 116 5 5 HELIX 33 AD6 TYR H 37 HIS H 49 1 13 HELIX 34 AD7 SER H 55 ASN H 84 1 30 HELIX 35 AD8 THR H 90 LEU H 102 1 13 HELIX 36 AD9 GLY H 104 ALA H 124 1 21 HELIX 37 AE1 GLU M 98 THR M 102 5 5 HELIX 38 AE2 THR M 177 THR M 179 5 3 HELIX 39 AE3 GLU M 211 LYS M 214 5 4 HELIX 40 AE4 THR M 236 SER M 240 5 5 HELIX 41 AE5 GLU N 98 THR N 102 5 5 HELIX 42 AE6 THR N 177 THR N 179 5 3 HELIX 43 AE7 THR N 236 SER N 240 5 5 SHEET 1 AA1 2 ARG A 83 PHE A 84 0 SHEET 2 AA1 2 THR B 80 VAL B 81 1 O VAL B 81 N ARG A 83 SHEET 1 AA2 2 THR A 118 ILE A 119 0 SHEET 2 AA2 2 ARG B 45 ILE B 46 1 O ARG B 45 N ILE A 119 SHEET 1 AA3 2 LEU B 97 TYR B 98 0 SHEET 2 AA3 2 THR G 101 ILE G 102 1 O THR G 101 N TYR B 98 SHEET 1 AA4 2 ARG C 42 VAL C 43 0 SHEET 2 AA4 2 THR D 88 ILE D 89 1 O ILE D 89 N ARG C 42 SHEET 1 AA5 2 ARG C 77 ILE C 78 0 SHEET 2 AA5 2 GLY D 53 ILE D 54 1 O GLY D 53 N ILE C 78 SHEET 1 AA6 2 VAL C 100 ILE C 102 0 SHEET 2 AA6 2 THR F 96 TYR F 98 1 O TYR F 98 N THR C 101 SHEET 1 AA7 2 ARG E 83 PHE E 84 0 SHEET 2 AA7 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83 SHEET 1 AA8 2 THR E 118 ILE E 119 0 SHEET 2 AA8 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119 SHEET 1 AA9 2 ARG G 42 VAL G 43 0 SHEET 2 AA9 2 THR H 88 ILE H 89 1 O ILE H 89 N ARG G 42 SHEET 1 AB1 2 ARG G 77 ILE G 78 0 SHEET 2 AB1 2 GLY H 53 ILE H 54 1 O GLY H 53 N ILE G 78 SHEET 1 AB2 4 MET M 23 GLN M 25 0 SHEET 2 AB2 4 VAL M 38 ALA M 44 -1 O LYS M 43 N THR M 24 SHEET 3 AB2 4 ASP M 89 ILE M 94 -1 O LEU M 92 N ILE M 40 SHEET 4 AB2 4 PHE M 81 SER M 84 -1 N SER M 82 O THR M 93 SHEET 1 AB3 6 SER M 29 ALA M 32 0 SHEET 2 AB3 6 THR M 121 ILE M 125 1 O GLU M 124 N MET M 30 SHEET 3 AB3 6 ALA M 103 GLN M 109 -1 N ALA M 103 O LEU M 123 SHEET 4 AB3 6 LEU M 52 GLN M 57 -1 N SER M 53 O LEU M 108 SHEET 5 AB3 6 LYS M 64 TYR M 68 -1 O LYS M 64 N GLN M 56 SHEET 6 AB3 6 SER M 72 LEU M 73 -1 O SER M 72 N TYR M 68 SHEET 1 AB4 4 SER M 29 ALA M 32 0 SHEET 2 AB4 4 THR M 121 ILE M 125 1 O GLU M 124 N MET M 30 SHEET 3 AB4 4 ALA M 103 GLN M 109 -1 N ALA M 103 O LEU M 123 SHEET 4 AB4 4 THR M 116 PHE M 117 -1 O THR M 116 N GLN M 109 SHEET 1 AB5 4 GLN M 152 GLN M 155 0 SHEET 2 AB5 4 VAL M 167 SER M 174 -1 O LYS M 172 N GLN M 154 SHEET 3 AB5 4 THR M 227 LEU M 232 -1 O MET M 230 N MET M 169 SHEET 4 AB5 4 ALA M 217 ASP M 222 -1 N ASP M 222 O THR M 227 SHEET 1 AB6 6 GLU M 159 VAL M 161 0 SHEET 2 AB6 6 THR M 263 VAL M 267 1 O THR M 266 N GLU M 159 SHEET 3 AB6 6 ALA M 241 SER M 249 -1 N TYR M 243 O THR M 263 SHEET 4 AB6 6 TYR M 181 THR M 189 -1 N GLN M 184 O ALA M 246 SHEET 5 AB6 6 GLY M 193 ILE M 200 -1 O GLU M 195 N LYS M 187 SHEET 6 AB6 6 THR M 207 TYR M 209 -1 O LYS M 208 N TYR M 199 SHEET 1 AB7 4 GLU M 159 VAL M 161 0 SHEET 2 AB7 4 THR M 263 VAL M 267 1 O THR M 266 N GLU M 159 SHEET 3 AB7 4 ALA M 241 SER M 249 -1 N TYR M 243 O THR M 263 SHEET 4 AB7 4 TYR M 258 TRP M 259 -1 O TYR M 258 N ARG M 247 SHEET 1 AB8 4 MET N 23 GLN N 25 0 SHEET 2 AB8 4 VAL N 38 ALA N 44 -1 O LYS N 43 N THR N 24 SHEET 3 AB8 4 ASP N 89 ILE N 94 -1 O LEU N 92 N ILE N 40 SHEET 4 AB8 4 PHE N 81 SER N 86 -1 N SER N 82 O THR N 93 SHEET 1 AB9 6 SER N 29 ALA N 32 0 SHEET 2 AB9 6 THR N 121 ILE N 125 1 O LYS N 122 N MET N 30 SHEET 3 AB9 6 ALA N 103 GLN N 109 -1 N TYR N 105 O THR N 121 SHEET 4 AB9 6 LEU N 52 GLN N 57 -1 N SER N 53 O LEU N 108 SHEET 5 AB9 6 PRO N 63 TYR N 68 -1 O LEU N 66 N TRP N 54 SHEET 6 AB9 6 SER N 72 LEU N 73 -1 O SER N 72 N TYR N 68 SHEET 1 AC1 4 SER N 29 ALA N 32 0 SHEET 2 AC1 4 THR N 121 ILE N 125 1 O LYS N 122 N MET N 30 SHEET 3 AC1 4 ALA N 103 GLN N 109 -1 N TYR N 105 O THR N 121 SHEET 4 AC1 4 THR N 116 PHE N 117 -1 O THR N 116 N GLN N 109 SHEET 1 AC2 4 GLN N 152 GLN N 155 0 SHEET 2 AC2 4 VAL N 167 SER N 174 -1 O LYS N 172 N GLN N 154 SHEET 3 AC2 4 THR N 227 LEU N 232 -1 O MET N 230 N MET N 169 SHEET 4 AC2 4 ALA N 217 ASP N 222 -1 N THR N 220 O TYR N 229 SHEET 1 AC3 6 GLU N 159 VAL N 161 0 SHEET 2 AC3 6 THR N 263 VAL N 267 1 O SER N 264 N GLU N 159 SHEET 3 AC3 6 VAL N 242 SER N 249 -1 N TYR N 243 O THR N 263 SHEET 4 AC3 6 TYR N 181 THR N 189 -1 N GLN N 184 O ALA N 246 SHEET 5 AC3 6 GLY N 193 ILE N 200 -1 O GLU N 195 N LYS N 187 SHEET 6 AC3 6 THR N 207 TYR N 209 -1 O LYS N 208 N TYR N 199 SHEET 1 AC4 4 GLU N 159 VAL N 161 0 SHEET 2 AC4 4 THR N 263 VAL N 267 1 O SER N 264 N GLU N 159 SHEET 3 AC4 4 VAL N 242 SER N 249 -1 N TYR N 243 O THR N 263 SHEET 4 AC4 4 TYR N 258 TRP N 259 -1 O TYR N 258 N ARG N 247 SSBOND 1 CYS M 42 CYS M 107 1555 1555 2.04 SSBOND 2 CYS M 171 CYS M 245 1555 1555 2.03 SSBOND 3 CYS N 42 CYS N 107 1555 1555 2.03 SSBOND 4 CYS N 171 CYS N 245 1555 1555 2.03 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000